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- EMDB-17191: The H/ACA RNP lobe of human telomerase with the dyskerin thumb lo... -

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Basic information

Entry
Database: EMDB / ID: EMD-17191
TitleThe H/ACA RNP lobe of human telomerase with the dyskerin thumb loop in an open conformation
Map dataFinal post-processed sharpened map.
Sample
  • Complex: Human telomerase H/ACA RNP lobe
    • Complex: Telomerase H/ACA RNP lobe
      • Protein or peptide: H/ACA ribonucleoprotein complex subunit DKC1
      • Protein or peptide: H/ACA ribonucleoprotein complex subunit 1
      • Protein or peptide: H/ACA ribonucleoprotein complex subunit 2
      • Protein or peptide: H/ACA ribonucleoprotein complex subunit 3
      • Protein or peptide: Telomerase Cajal body protein 1
    • Complex: Human telomerase RNATelomerase RNA component
      • RNA: Human telomerase RNATelomerase RNA component
Keywordstelomerase / H/ACA / pseudouridylation / ribonucleoprotein / RNA BINDING PROTEIN
Function / homology
Function and homology information


telomere formation via telomerase / box H/ACA scaRNP complex / box H/ACA telomerase RNP complex / telomerase RNA localization to Cajal body / protein localization to Cajal body / Cajal body organization / snoRNA guided rRNA pseudouridine synthesis / box H/ACA snoRNP complex / rRNA pseudouridine synthesis / box H/ACA sno(s)RNA 3'-end processing ...telomere formation via telomerase / box H/ACA scaRNP complex / box H/ACA telomerase RNP complex / telomerase RNA localization to Cajal body / protein localization to Cajal body / Cajal body organization / snoRNA guided rRNA pseudouridine synthesis / box H/ACA snoRNP complex / rRNA pseudouridine synthesis / box H/ACA sno(s)RNA 3'-end processing / snRNA pseudouridine synthesis / Isomerases; Intramolecular transferases; Transferring other groups / mRNA pseudouridine synthesis / enzyme-directed rRNA pseudouridine synthesis / pseudouridine synthesis / telomerase RNA stabilization / telomerase activity / box H/ACA snoRNA binding / regulation of telomerase RNA localization to Cajal body / pseudouridine synthase activity / scaRNA localization to Cajal body / positive regulation of protein localization to Cajal body / positive regulation of establishment of protein localization to telomere / positive regulation of telomerase RNA localization to Cajal body / sno(s)RNA-containing ribonucleoprotein complex / telomerase RNA binding / telomerase holoenzyme complex / rRNA modification in the nucleus and cytosol / positive regulation of double-strand break repair / positive regulation of double-strand break repair via homologous recombination / positive regulation of double-strand break repair via nonhomologous end joining / Association of TriC/CCT with target proteins during biosynthesis / RNA folding / Telomere Extension By Telomerase / telomere maintenance via telomerase / Cajal body / RNA processing / maturation of LSU-rRNA / positive regulation of telomerase activity / positive regulation of DNA repair / positive regulation of telomere maintenance via telomerase / fibrillar center / rRNA processing / site of double-strand break / cytosolic large ribosomal subunit / histone binding / protein-folding chaperone binding / chromosome, telomeric region / nuclear body / DNA repair / ubiquitin protein ligase binding / protein-containing complex binding / nucleolus / RNA binding / nucleoplasm / identical protein binding / nucleus / cytosol / cytoplasm
Similarity search - Function
H/ACA ribonucleoprotein complex, subunit Gar1/Naf1 / H/ACA RNP complex subunit Gar1/Naf1, Cbf5-binding domain / Gar1/Naf1 RNA binding region / tRNA pseudouridine synthase B family / Dyskerin-like / DKCLD (NUC011) domain / DKCLD (NUC011) domain / H/ACA ribonucleoprotein complex, subunit Nop10 / H/ACA ribonucleoprotein complex, subunit Nop10 superfamily / Nucleolar RNA-binding protein, Nop10p family ...H/ACA ribonucleoprotein complex, subunit Gar1/Naf1 / H/ACA RNP complex subunit Gar1/Naf1, Cbf5-binding domain / Gar1/Naf1 RNA binding region / tRNA pseudouridine synthase B family / Dyskerin-like / DKCLD (NUC011) domain / DKCLD (NUC011) domain / H/ACA ribonucleoprotein complex, subunit Nop10 / H/ACA ribonucleoprotein complex, subunit Nop10 superfamily / Nucleolar RNA-binding protein, Nop10p family / Pseudouridine synthase II, N-terminal / tRNA pseudouridylate synthase B, C-terminal / TruB family pseudouridylate synthase (N terminal domain) / tRNA pseudouridylate synthase B C-terminal domain / Uncharacterised domain CHP00451 / PUA domain / Pseudouridine synthase, catalytic domain superfamily / Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase / PUA domain / PUA domain profile. / PUA domain superfamily / H/ACA ribonucleoprotein complex, subunit Nhp2-like / PUA-like superfamily / Ribosomal protein L7Ae/L8/Nhp2 family / Ribosomal protein L7Ae/L30e/S12e/Gadd45 / Ribosomal protein L7Ae/L30e/S12e/Gadd45 family / 50S ribosomal protein L30e-like / Translation protein, beta-barrel domain superfamily / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily
Similarity search - Domain/homology
H/ACA ribonucleoprotein complex subunit DKC1 / Telomerase Cajal body protein 1 / H/ACA ribonucleoprotein complex subunit 3 / H/ACA ribonucleoprotein complex subunit 2 / H/ACA ribonucleoprotein complex subunit 1
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.1 Å
AuthorsGhanim GE / Sekne Z / van Roon AMM / Balch S / Nguyen THD
Funding support United Kingdom, United States, European Union, 3 items
OrganizationGrant numberCountry
UK Research and Innovation (UKRI)MC_UP_1201/19 United Kingdom
Jane Coffin Childs (JCC) Fund United States
European Molecular Biology Organization (EMBO)European Union
CitationJournal: Nat Commun / Year: 2024
Title: 2.7 Å cryo-EM structure of human telomerase H/ACA ribonucleoprotein.
Authors: George E Ghanim / Zala Sekne / Sebastian Balch / Anne-Marie M van Roon / Thi Hoang Duong Nguyen /
Abstract: Telomerase is a ribonucleoprotein (RNP) enzyme that extends telomeric repeats at eukaryotic chromosome ends to counterbalance telomere loss caused by incomplete genome replication. Human telomerase ...Telomerase is a ribonucleoprotein (RNP) enzyme that extends telomeric repeats at eukaryotic chromosome ends to counterbalance telomere loss caused by incomplete genome replication. Human telomerase is comprised of two distinct functional lobes tethered by telomerase RNA (hTR): a catalytic core, responsible for DNA extension; and a Hinge and ACA (H/ACA) box RNP, responsible for telomerase biogenesis. H/ACA RNPs also have a general role in pseudouridylation of spliceosomal and ribosomal RNAs, which is critical for the biogenesis of the spliceosome and ribosome. Much of our structural understanding of eukaryotic H/ACA RNPs comes from structures of the human telomerase H/ACA RNP. Here we report a 2.7 Å cryo-electron microscopy structure of the telomerase H/ACA RNP. The significant improvement in resolution over previous 3.3 Å to 8.2 Å structures allows us to uncover new molecular interactions within the H/ACA RNP. Many disease mutations are mapped to these interaction sites. The structure also reveals unprecedented insights into a region critical for pseudouridylation in canonical H/ACA RNPs. Together, our work advances understanding of telomerase-related disease mutations and the mechanism of pseudouridylation by eukaryotic H/ACA RNPs.
History
DepositionApr 22, 2023-
Header (metadata) releaseJan 31, 2024-
Map releaseJan 31, 2024-
UpdateFeb 7, 2024-
Current statusFeb 7, 2024Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_17191.png

Downloads & links

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Map

FileDownload / File: emd_17191.map.gz / Format: CCP4 / Size: 83.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationFinal post-processed sharpened map.
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.06 Å/pix.
x 280 pix.
= 296.52 Å		1.06 Å/pix.
x 280 pix.
= 296.52 Å		1.06 Å/pix.
x 280 pix.
= 296.52 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.059 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.028
Minimum - Maximum-0.08476315 - 0.16979967
Average (Standard dev.)-0.000026646661 (±0.004614141)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions280280280
Spacing280280280
CellA=B=C: 296.52002 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: Final unsharped map.

Fileemd_17191_additional_1.map
AnnotationFinal unsharped map.
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half-map2 resulting from gold standard refinement in RELION.

Fileemd_17191_half_map_1.map
AnnotationHalf-map2 resulting from gold standard refinement in RELION.
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half-map1 resulting from gold standard refinement in RELION.

Fileemd_17191_half_map_2.map
AnnotationHalf-map1 resulting from gold standard refinement in RELION.
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Human telomerase H/ACA RNP lobe

EntireName: Human telomerase H/ACA RNP lobe
Components
  • Complex: Human telomerase H/ACA RNP lobe
    • Complex: Telomerase H/ACA RNP lobe
      • Protein or peptide: H/ACA ribonucleoprotein complex subunit DKC1
      • Protein or peptide: H/ACA ribonucleoprotein complex subunit 1
      • Protein or peptide: H/ACA ribonucleoprotein complex subunit 2
      • Protein or peptide: H/ACA ribonucleoprotein complex subunit 3
      • Protein or peptide: Telomerase Cajal body protein 1
    • Complex: Human telomerase RNATelomerase RNA component
      • RNA: Human telomerase RNATelomerase RNA component

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Supramolecule #1: Human telomerase H/ACA RNP lobe

SupramoleculeName: Human telomerase H/ACA RNP lobe / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Details: The hTR H/ACA motif, which adopts a double-hairpin structure hinged by the H-box and flanked by the ACA box, scaffolds the assembly of two copies each of dyskerin, NHP2, NOP10 and GAR1, one ...Details: The hTR H/ACA motif, which adopts a double-hairpin structure hinged by the H-box and flanked by the ACA box, scaffolds the assembly of two copies each of dyskerin, NHP2, NOP10 and GAR1, one on each hairpin. TCAB1 binds the CAB box.
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 415 KDa

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Supramolecule #2: Telomerase H/ACA RNP lobe

SupramoleculeName: Telomerase H/ACA RNP lobe / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #2-#6
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #3: Human telomerase RNA

SupramoleculeName: Human telomerase RNA / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #1
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Human telomerase RNA

MacromoleculeName: Human telomerase RNA / type: rna / ID: 1 / Number of copies: 1
Source (natural)Organism: Homo sapiens (human) / Organ: Kidney
Molecular weightTheoretical: 145.477797 KDa
SequenceString: GGGUUGCGGA GGGUGGGCCU GGGAGGGGUG GUGGCCAUUU UUUGUCUAAC CCUAACUGAG AAGGGCGUAG GCGCCGUGCU UUUGCUCCC CGCGCGCUGU UUUUCUCGCU GACUUUCAGC GGGCGGAAAA GCCUCGGCCU GCCGCCUUCC ACCGUUCAUU C UAGAGCAA ...String:
GGGUUGCGGA GGGUGGGCCU GGGAGGGGUG GUGGCCAUUU UUUGUCUAAC CCUAACUGAG AAGGGCGUAG GCGCCGUGCU UUUGCUCCC CGCGCGCUGU UUUUCUCGCU GACUUUCAGC GGGCGGAAAA GCCUCGGCCU GCCGCCUUCC ACCGUUCAUU C UAGAGCAA ACAAAAAAUG UCAGCUGCUG GCCCGUUCGC CCCUCCCGGG GACCUGCGGC GGGUCGCCUG CCCAGCCCCC GA ACCCCGC CUGGAGGCCG CGGUCGGCCC GGGGCUUCUC CGGAGGCACC CACUGCCACC GCGAAGAGUU GGGCUCUGUC AGC CGCGGG UCUCUCGGGG GCGAGGGCGA GGUUCAGGCC UUUCAGGCCG CAGGAAGAGG AACGGAGCGA GUCCCCGCGC GCGG CGCGA UUCCCUGAGC UGUGGGACGU GCACCCAGGA CUCGGCUCAC ACAUGC

GENBANK: GENBANK: U85256.1

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Macromolecule #2: H/ACA ribonucleoprotein complex subunit DKC1

MacromoleculeName: H/ACA ribonucleoprotein complex subunit DKC1 / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Organ: Kidney
Molecular weightTheoretical: 57.779211 KDa
SequenceString: MADAEVIILP KKHKKKKERK SLPEEDVAEI QHAEEFLIKP ESKVAKLDTS QWPLLLKNFD KLNVRTTHYT PLACGSNPLK REIGDYIRT GFINLDKPSN PSSHEVVAWI RRILRVEKTG HSGTLDPKVT GCLIVCIERA TRLVKSQQSA GKEYVGIVRL H NAIEGGTQ ...String:
MADAEVIILP KKHKKKKERK SLPEEDVAEI QHAEEFLIKP ESKVAKLDTS QWPLLLKNFD KLNVRTTHYT PLACGSNPLK REIGDYIRT GFINLDKPSN PSSHEVVAWI RRILRVEKTG HSGTLDPKVT GCLIVCIERA TRLVKSQQSA GKEYVGIVRL H NAIEGGTQ LSRALETLTG ALFQRPPLIA AVKRQLRVRT IYESKMIEYD PERRLGIFWV SCEAGTYIRT LCVHLGLLLG VG GQMQELR RVRSGVMSEK DHMVTMHDVL DAQWLYDNHK DESYLRRVVY PLEKLLTSHK RLVMKDSAVN AICYGAKIML PGV LRYEDG IEVNQEIVVI TTKGEAICMA IALMTTAVIS TCDHGIVAKI KRVIMERDTY PRKWGLGPKA SQKKLMIKQG LLDK HGKPT DSTPATWKQE YVDYSESAKK EVVAEVVKAP QVVAEAAKTA KRKRESESES DETPPAAPQL IKKEKKKSKK DKKAK AGLE SGAEPGDGDS DTTKKKKKKK KAKEVELVSE

UniProtKB: H/ACA ribonucleoprotein complex subunit DKC1

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Macromolecule #3: H/ACA ribonucleoprotein complex subunit 1

MacromoleculeName: H/ACA ribonucleoprotein complex subunit 1 / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Organ: Kidney
Molecular weightTheoretical: 22.387963 KDa
SequenceString: MSFRGGGRGG FNRGGGGGGF NRGGSSNHFR GGGGGGGGGN FRGGGRGGFG RGGGRGGFNK GQDQGPPERV VLLGEFLHPC EDDIVCKCT TDENKVPYFN APVYLENKEQ IGKVDEIFGQ LRDFYFSVKL SENMKASSFK KLQKFYIDPY KLLPLQRFLP R PPGEKGPP ...String:
MSFRGGGRGG FNRGGGGGGF NRGGSSNHFR GGGGGGGGGN FRGGGRGGFG RGGGRGGFNK GQDQGPPERV VLLGEFLHPC EDDIVCKCT TDENKVPYFN APVYLENKEQ IGKVDEIFGQ LRDFYFSVKL SENMKASSFK KLQKFYIDPY KLLPLQRFLP R PPGEKGPP RGGGRGGRGG GRGGGGRGGG RGGGFRGGRG GGGGGFRGGR GGGFRGRGH

UniProtKB: H/ACA ribonucleoprotein complex subunit 1

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Macromolecule #4: H/ACA ribonucleoprotein complex subunit 2

MacromoleculeName: H/ACA ribonucleoprotein complex subunit 2 / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Organ: Kidney
Molecular weightTheoretical: 17.22607 KDa
SequenceString:
MTKIKADPDG PEAQAEACSG ERTYQELLVN QNPIAQPLAS RRLTRKLYKC IKKAVKQKQI RRGVKEVQKF VNKGEKGIMV LAGDTLPIE VYCHLPVMCE DRNLPYVYIP SKTDLGAAAG SKRPTCVIMV KPHEEYQEAY DECLEEVQSL PLPL

UniProtKB: H/ACA ribonucleoprotein complex subunit 2

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Macromolecule #5: H/ACA ribonucleoprotein complex subunit 3

MacromoleculeName: H/ACA ribonucleoprotein complex subunit 3 / type: protein_or_peptide / ID: 5 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Organ: Kidney
Molecular weightTheoretical: 7.719989 KDa
SequenceString:
MFLQYYLNEQ GDRVYTLKKF DPMGQQTCSA HPARFSPDDK YSRHRITIKK RFKVLMTQQP RPVL

UniProtKB: H/ACA ribonucleoprotein complex subunit 3

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Macromolecule #6: Telomerase Cajal body protein 1

MacromoleculeName: Telomerase Cajal body protein 1 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Organ: Kidney
Molecular weightTheoretical: 59.35707 KDa
SequenceString: MKTLETQPLA PDCCPSDQDP APAHPSPHAS PMNKNADSEL MPPPPERGDP PRLSPDPVAG SAVSQELREG DPVSLSTPLE TEFGSPSEL SPRIEEQELS ENTSLPAEEA NGSLSEEEAN GPELGSGKAM EDTSGEPAAE DEGDTAWNYS FSQLPRFLSG S WSEFSTQP ...String:
MKTLETQPLA PDCCPSDQDP APAHPSPHAS PMNKNADSEL MPPPPERGDP PRLSPDPVAG SAVSQELREG DPVSLSTPLE TEFGSPSEL SPRIEEQELS ENTSLPAEEA NGSLSEEEAN GPELGSGKAM EDTSGEPAAE DEGDTAWNYS FSQLPRFLSG S WSEFSTQP ENFLKGCKWA PDGSCILTNS ADNILRIYNL PPELYHEGEQ VEYAEMVPVL RMVEGDTIYD YCWYSLMSSA QP DTSYVAS SSRENPIHIW DAFTGELRAS FRAYNHLDEL TAAHSLCFSP DGSQLFCGFN RTVRVFSTAR PGRDCEVRAT FAK KQGQSG IISCIAFSPA QPLYACGSYG RSLGLYAWDD GSPLALLGGH QGGITHLCFH PDGNRFFSGA RKDAELLCWD LRQS GYPLW SLGREVTTNQ RIYFDLDPTG QFLVSGSTSG AVSVWDTDGP GNDGKPEPVL SFLPQKDCTN GVSLHPSLPL LATAS GQRV FPEPTESGDE GEELGLPLLS TRHVHLECRL QLWWCGGAPD SSIPDDHQGE KGQGGTEGGV GELI

UniProtKB: Telomerase Cajal body protein 1

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 8
Component:
ConcentrationFormulaName
20.0 mMC8H18N2O4SHEPES
150.0 mMNaClSodium chlorideSodium chloride
2.0 mMMgCl2Magnesium chloride
0.05 %(C2H4O)nC14H22OIgepal CA630
1.0 %C12H22O11Trehalose
1.0 mMC4H10O2S2DTT
GridModel: C-flat / Material: COPPER / Mesh: 400 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Support film - Film thickness: 5 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 12 sec. / Pretreatment - Atmosphere: AIR
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 50.0 µm / Calibrated magnification: 45872 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 81000
Specialist opticsEnergy filter - Name: GIF Quantum LS / Energy filter - Slit width: 20 eV
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
TemperatureMin: 78.0 K
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Digitization - Dimensions - Width: 5760 pixel / Digitization - Dimensions - Height: 4092 pixel / Number grids imaged: 2 / Number real images: 41053 / Average exposure time: 3.0 sec. / Average electron dose: 48.0 e/Å2
Details: Images were collected in movie-mode and fractionated into 48 movie frames
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 18744992
Startup modelType of model: OTHER
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 4)
Final 3D classificationSoftware - Name: RELION (ver. 4)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 4)
Final reconstructionNumber classes used: 1 / Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 4) / Number images used: 145627
DetailsAll images were processed using RELION4.0 and CryoSPARC 4.1.2
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelPDB ID:

7bgb


Chain - Source name: PDB / Chain - Initial model type: experimental model
Output model

PDB-8ouf:
The H/ACA RNP lobe of human telomerase with the dyskerin thumb loop in an open conformation

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